A Chaperone Complex Formed by HSP47, FKBP65, and BiP Modulates Telopeptide Lysyl Hydroxylation of Type I Procollagen.

作者: Ivan Duran , Jorge H Martin , Mary Ann Weis , Pavel Krejci , Peter Konik

DOI: 10.1002/JBMR.3095

关键词:

摘要: Lysine hydroxylation of type I collagen telopeptides varies from tissue to tissue, and these distinct patterns modulate cross-linking generate a unique extracellular matrix. Abnormalities in contribute pathologies that include osteogenesis imperfecta (OI), fibrosis, cancer. Telopeptide procollagen modifications are carried out by lysyl hydroxylase 2 (LH2); however, little is known regarding how this enzyme regulates patterns. We identified an ER complex resident chaperones includes HSP47, FKBP65, BiP regulating the activity LH2. Our findings show FKBP65 HSP47 LH2 either favor or repress its activity. was also as member complex, playing role enhancing formation complex. This newly chaperone contributes our understanding C-telopeptides affect quality connective tissues. © 2017 American Society for Bone Mineral Research.

参考文章(40)
Uschi Lindert, Mary Ann Weis, Jyoti Rai, Frank Seeliger, Ingrid Hausser, Tosso Leeb, David Eyre, Marianne Rohrbach, Cecilia Giunta, Molecular Consequences of the SERPINH1/HSP47 Mutation in the Dachshund Natural Model of Osteogenesis Imperfecta Journal of Biological Chemistry. ,vol. 290, pp. 17679- 17689 ,(2015) , 10.1074/JBC.M115.661025
Roy Morello, Terry K. Bertin, Yuqing Chen, John Hicks, Laura Tonachini, Massimiliano Monticone, Patrizio Castagnola, Frank Rauch, Francis H. Glorieux, Janice Vranka, Hans Peter Bächinger, James M. Pace, Ulrike Schwarze, Peter H. Byers, MaryAnn Weis, Russell J. Fernandes, David R. Eyre, Zhenqiang Yao, Brendan F. Boyce, Brendan Lee, CRTAP is required for prolyl 3- hydroxylation and mutations cause recessive osteogenesis imperfecta. Cell. ,vol. 127, pp. 291- 304 ,(2006) , 10.1016/J.CELL.2006.08.039
David R. Eyre, Mary Ann Weis, Bone collagen: new clues to its mineralization mechanism from recessive osteogenesis imperfecta. Calcified Tissue International. ,vol. 93, pp. 338- 347 ,(2013) , 10.1007/S00223-013-9723-9
Mitsuo Yamauchi, Marnisa Sricholpech, Lysine post-translational modifications of collagen. Essays in Biochemistry. ,vol. 52, pp. 113- 133 ,(2012) , 10.1042/BSE0520113
Irene Weibrecht, Karl-Johan Leuchowius, Carl-Magnus Clausson, Tim Conze, Malin Jarvius, W Mathias Howell, Masood Kamali-Moghaddam, Ola Söderberg, Proximity ligation assays : a recent addition to the proteomics toolbox Expert Review of Proteomics. ,vol. 7, pp. 401- 409 ,(2010) , 10.1586/EPR.10.10
Aileen M. Barnes, Wayne A. Cabral, MaryAnn Weis, Elena Makareeva, Edward L. Mertz, Sergey Leikin, David Eyre, Carlos Trujillo, Joan C. Marini, Absence of FKBP10 in recessive type XI osteogenesis imperfecta leads to diminished collagen cross-linking and reduced collagen deposition in extracellular matrix. Human Mutation. ,vol. 33, pp. 1589- 1598 ,(2012) , 10.1002/HUMU.22139
Shireen R. Lamandé, Steven D. Chessler, Suzanne B. Golub, Peter H. Byers, Chan Chan, William G. Cole, David O. Sillence, John F. Bateman, Endoplasmic reticulum-mediated quality control of type I collagen production by cells from osteogenesis imperfecta patients with mutations in the pro alpha 1 (I) chain carboxyl-terminal propeptide which impair subunit assembly Journal of Biological Chemistry. ,vol. 270, pp. 8642- 8649 ,(1995) , 10.1074/JBC.270.15.8642
Brian P Kelley, Fransiska Malfait, Luisa Bonafe, Dustin Baldridge, Erica Homan, Sofie Symoens, Andy Willaert, Nursel Elcioglu, Lionel Van Maldergem, Christine Verellen-Dumoulin, Yves Gillerot, Dobrawa Napierala, Deborah Krakow, Peter Beighton, Andrea Superti-Furga, Anne De Paepe, Brendan Lee, Mutations in FKBP10 Cause Recessive Osteogenesis Imperfecta and Bruck Syndrome Journal of Bone and Mineral Research. ,vol. 26, pp. 666- 672 ,(2011) , 10.1002/JBMR.250